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3swd

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==E. coli MurA in complex with UDP-N-acetylmuramic acid and covalent adduct of PEP with Cys115==
==E. coli MurA in complex with UDP-N-acetylmuramic acid and covalent adduct of PEP with Cys115==
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<StructureSection load='3swd' size='340' side='right' caption='[[3swd]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='3swd' size='340' side='right'caption='[[3swd]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3swd]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SWD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SWD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3swd]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SWD FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPZ:(2R)-2-{[(2R,3R,4R,5S,6R)-3-(ACETYLAMINO)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-DIOXO-3,4-DIHYDROPYRIMIDIN-1(2H)-YL)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL]METHOXY}(HYDROXY)PHOSPHORYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-5-HYDROXY-6-(HYDROXYMETHYL)TETRAHYDRO-2H-PYRAN-4-YL]OXY}PROPANOIC+ACID'>EPZ</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IAS:BETA-L-ASPARTIC+ACID'>IAS</scene>, <scene name='pdbligand=QPA:S-[(1S)-1-CARBOXY-1-(PHOSPHONOOXY)ETHYL]-L-CYSTEINE'>QPA</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPZ:(2R)-2-{[(2R,3R,4R,5S,6R)-3-(ACETYLAMINO)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-DIOXO-3,4-DIHYDROPYRIMIDIN-1(2H)-YL)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL]METHOXY}(HYDROXY)PHOSPHORYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-5-HYDROXY-6-(HYDROXYMETHYL)TETRAHYDRO-2H-PYRAN-4-YL]OXY}PROPANOIC+ACID'>EPZ</scene>, <scene name='pdbligand=IAS:BETA-L-ASPARTIC+ACID'>IAS</scene>, <scene name='pdbligand=QPA:S-[(1S)-1-CARBOXY-1-(PHOSPHONOOXY)ETHYL]-L-CYSTEINE'>QPA</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3iss|3iss]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3swd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3swd OCA], [https://pdbe.org/3swd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3swd RCSB], [https://www.ebi.ac.uk/pdbsum/3swd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3swd ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b3189, JW3156, murA, murZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
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</table>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_1-carboxyvinyltransferase UDP-N-acetylglucosamine 1-carboxyvinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.7 2.5.1.7] </span></td></tr>
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== Function ==
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3swd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3swd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3swd RCSB], [http://www.ebi.ac.uk/pdbsum/3swd PDBsum]</span></td></tr>
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[https://www.uniprot.org/uniprot/MURA_ECOLI MURA_ECOLI] Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Target for the antibiotic phosphomycin.[HAMAP-Rule:MF_00111]
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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MurA (enolpyruvyl UDP-GlcNAc synthase) catalyzes the first committed step in peptidoglycan biosynthesis. In this study, MurA-catalyzed breakdown of its tetrahedral intermediate (THI), with a k(cat)/K(M) of 520 M(-1) s(-1), was far slower than the normal reaction, and 3 x 10(5)-fold slower than the homologous enzyme, AroA, reacting with its THI. This provided kinetic evidence of slow binding and a conformationally constrained active site. The MurA cocrystal structure with UDP-N-acetylmuramic acid (UDP-MurNAc), a potent inhibitor, and phosphite revealed a new "staged" MurA conformation in which the Arg397 side chain tracked phosphite out of the catalytic site. The closed-to-staged transition involved breaking eight MurA.ligand ion pairs, and three intraprotein hydrogen bonds helping hold the active site loop closed. These were replaced with only two MurA.UDP-MurNAc ion pairs, two with phosphite, and seven new intraprotein ion pairs or hydrogen bonds. Cys115 appears to have an important role in forming the staged conformation. The staged conformation appears to be one step in a complex choreography of release of the product from MurA.
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Evidence of Kinetic Control of Ligand Binding and Staged Product Release in MurA (Enolpyruvyl UDP-GlcNAc Synthase)-Catalyzed Reactions .,Jackson SG, Zhang F, Chindemi P, Junop MS, Berti PJ Biochemistry. 2009 Nov 18. PMID:19899805<ref>PMID:19899805</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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*[[Enoylpyruvate transferase|Enoylpyruvate transferase]]
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*[[Enoylpyruvate transferase 3D structures|Enoylpyruvate transferase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Escherichia coli K-12]]
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[[Category: UDP-N-acetylglucosamine 1-carboxyvinyltransferase]]
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[[Category: Large Structures]]
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[[Category: Schonbrunn, E.]]
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[[Category: Schonbrunn E]]
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[[Category: Zhu, J Y.]]
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[[Category: Zhu J-Y]]
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[[Category: Biogenesis/degradation]]
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[[Category: Cell wall]]
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[[Category: Close enzyme state]]
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[[Category: Mura]]
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[[Category: Peptidoglycan synthesis]]
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[[Category: Transferase]]
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Current revision

E. coli MurA in complex with UDP-N-acetylmuramic acid and covalent adduct of PEP with Cys115

PDB ID 3swd

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